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CCPG1_CHICK
ID   CCPG1_CHICK             Reviewed;         801 AA.
AC   Q5ZM60;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cell cycle progression protein 1;
GN   Name=CCPG1; ORFNames=RCJMB04_3a3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: May be involved in the regulation of Rho-mediated signaling
CC       pathways and in cell cycle regulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CCPG1 family. {ECO:0000305}.
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DR   EMBL; AJ719524; CAG31183.1; -; mRNA.
DR   RefSeq; NP_001026626.1; NM_001031455.1.
DR   AlphaFoldDB; Q5ZM60; -.
DR   SMR; Q5ZM60; -.
DR   STRING; 9031.ENSGALP00000007003; -.
DR   PaxDb; Q5ZM60; -.
DR   PRIDE; Q5ZM60; -.
DR   GeneID; 427496; -.
DR   KEGG; gga:427496; -.
DR   CTD; 9236; -.
DR   VEuPathDB; HostDB:geneid_427496; -.
DR   eggNOG; ENOG502QWDZ; Eukaryota.
DR   HOGENOM; CLU_018722_0_0_1; -.
DR   InParanoid; Q5ZM60; -.
DR   OrthoDB; 667993at2759; -.
DR   PhylomeDB; Q5ZM60; -.
DR   TreeFam; TF333202; -.
DR   PRO; PR:Q5ZM60; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:2001106; P:regulation of Rho guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   InterPro; IPR033588; CCPG1.
DR   PANTHER; PTHR28638:SF2; PTHR28638:SF2; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Coiled coil; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..801
FT                   /note="Cell cycle progression protein 1"
FT                   /id="PRO_0000310541"
FT   TOPO_DOM        1..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..801
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          79..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          285..449
FT                   /evidence="ECO:0000255"
FT   COILED          500..530
FT                   /evidence="ECO:0000255"
FT   COILED          695..726
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        81..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..780
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  93485 MW;  F963357351C43A8E CRC64;
     MSENYSDSDS SCGWTVINHE GSDIETVTSE NGSSNDNHEF VSEEYVSLQE VEQPIELQAQ
     DSTDGEIPVV DNTLSALEET QTVPEERKEK VHDDSSCIGT ISDDSDIVTL EAPKGEETPS
     QEEAPADGEE APSSEDFNMG SSSSSQYAFS QPETVFPSQA SDDESSSDET SNQSSPTVRR
     RRAKRRLISC SEAESGSPVG PEPEPPQEQQ HKRQFSSGLN RCIILALVIA ISMGFGHFYG
     TIQIQKRQQL LTKTRELKDD LYQCQQEQGD KVGSLKGDLA TCLTSTEVEK KSFESQKKSL
     AAENQHLRES LEKEEKALVS LQEELRKLRQ QIRNLEDKGT STESIVMENQ KLREHLEEEK
     QRNHNFRRQK ETLFAEAQML RRELDKERHV TEALKKELEQ LSSRQTPDSV NDDDTLRENE
     EIETLRGRLV ELEKKLNFEQ QRSDLWEKLY VEAKDLTEKQ EMNEKGQKRG AKGQSKSKKK
     SKESFFGSVK ETFDVMKNSA KEFVRHHKEK IKQAKEAVKE KLKKFSDSVK STFRHFKDTT
     KTILDEKEKK PNEKKYEANK KARTFYREHN LYENLKQSHY RRPNVPKDFR DGRRHHFTAF
     EKDTDSQKCL NDPLCSRKHQ FDLKGCSGIF ECANQEFVSL FNRVSDPIGV DEFNRLMRKY
     LQQVVHNFRH WRELENFINK FFHNGFFIHD QMLFTDFVND VKDYLEDMKE YQNKNEKVFD
     DLDKYIYRYY FQYDNSPQYG PSRPKRPSFT QTENPRHEKQ AQKYHHRNKR EGKWHKHGRT
     NGRHMANLEI ELGQLPFDPK Y
 
 
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